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Literature summary for 7.3.2.7 extracted from

  • Walmsley, A.R.; Zhou, T.; Borges-Walmsley, M.I.; Rosen, B.P.
    Antimonite regulation of the ATPase activity of ArsA, the catalytic subunit of the arsenical pump (2001), Biochem. J., 360, 589-597.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of recombinant enzyme with a His-tag Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ATP substrate inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.073
-
ATP pH 7.5, in absence of SbIII Escherichia coli
0.132
-
ATP pH 7.5, in presence of SbIII Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Escherichia coli ADP + phosphate
-
?

Synonyms

Synonyms Comment Organism
ArsA ATPase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
MgATP2- neccasary for the pump function Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.792
-
ATP pH 7.5, in absence of SbIII Escherichia coli
0.945
-
ATP pH 7.5, in presence of SbIII Escherichia coli